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Search for the role of eIF5A in endoplasmic reticulum stress using large-scale proteomic GFP screen

Grant number: 16/15621-9
Support Opportunities:Scholarships abroad - Research Internship - Master's degree
Effective date (Start): November 01, 2016
Effective date (End): April 30, 2017
Field of knowledge:Biological Sciences - Biochemistry - Molecular Biology
Principal Investigator:Sandro Roberto Valentini
Grantee:Angélica Hollunder Klippel
Supervisor: Brenda Jean Andrews
Host Institution: Faculdade de Ciências Farmacêuticas (FCFAR). Universidade Estadual Paulista (UNESP). Campus de Araraquara. Araraquara , SP, Brazil
Research place: University of Toronto (U of T), Canada  
Associated to the scholarship:15/07728-5 - Analysis of the functional relationship between eIF5A and the transcription factor Hac1 in Saccharomyces cerevisiae, BP.MS


The translation factor 5A (eIF5A) is highly conserved in Archaea and eukaryotes and is essential for cell viability. This is the only protein known to contain the amino acid residue hypusine, essential for eIF5A function, generated by a post-translational modification. Although it was initially suggested a function for eIF5A in the translation initiation, it was in the elongation step that eIF5A function was better demonstrated. Recent data from our group revealed a possible role for eIF5A in the secretory pathway and endoplasmic reticulum (ER) translocation, suggesting an involvement for eIF5A on the translation of specific mRNAs related to these pathways. In addition, it has been suggested an activation of the ER stress response upon eIF5A depletion in mammalian cells. Interestingly, our laboratory have some unpublished data demonstrating that yeast eIF5A mutants are sensitive to dithiothreitol (DTT) and resistant to tunicamycin, both drugs that activate the ER stress response upon. To better understand this dual behavior of eIF5A mutants, we propose here the use of the S. cerevisiae GFP collection for a proteomic screen upon induction of ER stress by DTT and tunicamycin. Therefore, the resulting protein abundance data will contribute to determine how eIF5A function correlates with the ER stress, and also to the general role of eIF5A during gene expression. (AU)

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